4.7 Article

Impact of Physicochemical Modifications in Casein Promoted by UV-C on the Peptide Profile of Gastric Digestion and the Transepithelial Transport of Peptides

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 71, Issue 19, Pages 7495-7507

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.3c00392

Keywords

micellar casein isolate; ultraviolet light irradiation; particle size and spectroscopic analyses; in vitro protein digestibility; peptide sequencing

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Caseins, the main proteins in milk, have a slow digestion rate due to their structure. Ultraviolet light irradiation (UV-C) can induce structural changes in casein and affect its allergenicity. Spectroscopic techniques revealed alterations in the micelle structure of casein after UV-C exposure. UV-C also led to changes in particle size distribution. However, UV-C did not impact peptide formation and transport in the Caco-2 cell model, although certain opioid peptides were affected. This study demonstrates that UV-C can be used to modify dairy products, promoting faster digestion and reducing allergenicity.
Caseins are the main proteins in milk, and their structure and spatial conformation are responsible for their slow digestion rate. The release of bioactive and beta-casomorphin peptides from casein digestion may induce allergic responses during consumption. Spectroscopic techniques were used to observe the structural changes in casein conformation induced by Ultraviolet light irradiation (UV-C). Raman spectroscopy results showed more pronounced peaks at 618 and 640 cm-1 for phenylalanine and tyrosine moieties of the photolyzed micellar casein, respectively, suggesting changes in the micelle structure. The decrease in the intensity of Raman signals for tryptophan and tyrosine corroborates to the UV-C-induced modifications of the micelle structure. Particle size distribution showed a decrease in the average micelle size after 15 min of UV-C exposure, while low-temperature, longtime (LTLT) pasteurization led to the formation of large aggregates, as observed by atomic force microscopy. UV-C did not impact the formation or transport of peptides, as observed by using the Caco-2 cell as a model for peptide absorption. However, the absence of the opioid peptide SRYPSY from kappa-casein and only 20% of the concentration of opioid peptide RYLGY were noted. This work demonstrated that UV-C can be utilized to induce the physicochemical modification of dairy products, promoting a higher digestion rate and reducing allergenicity.

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